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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
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- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제17권 제7호
- 발행연도
- 2007.1
- 수록면
- 1,098 - 1,105 (8page)
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simulation analysis has been performed on the model system forCALB (Candida antarctica lipase B) with esters to study thereaction mechanism and conformational preference of catalytichydrolysis and the esterification reaction. Using quantummechanical analysis, the ping-pong bi-bi mechanism was appliedand energies and 3-dimensional binding configurations of thewhole reaction pathways were calculated. Further moleculardynamics simulation analysis was performed on the basis ofthe transition state obtained from quantum mechanical study toobserve the effect of structures of the substrates. Calculationresults using substrates of diferent chain length and chiralconfigurations were compared for conformational preference.The calculated results showed very small influence on chainlength, whereas chiral conformation showed big diferences.Calculated results from molecular modeling studies havebeen compared qualitatively with the experimental data usingethyl acetate as substrates.
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